MCFD2_RAT
ID MCFD2_RAT Reviewed; 145 AA.
AC Q8K5B3;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Multiple coagulation factor deficiency protein 2 homolog;
DE AltName: Full=Neural stem cell-derived neuronal survival protein;
DE Flags: Precursor;
GN Name=Mcfd2; Synonyms=Sdnsf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344;
RA Toda H., Tashiro K., Takahashi J., Hashimoto N., Nakano I., Kobuke K.,
RA Tsuji M., Honjo T.;
RT "Isolation and characterization of SDNSF, a novel secretory molecule with
RT neuronal survival effect, from adult rat hippocampal stem cells.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: The MCFD2-LMAN1 complex forms a specific cargo receptor for
CC the ER-to-Golgi transport of selected proteins. {ECO:0000250}.
CC -!- SUBUNIT: Interacts in a calcium-dependent manner with LMAN1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus {ECO:0000250}.
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DR EMBL; AF475282; AAM28463.1; -; mRNA.
DR RefSeq; NP_640346.1; NM_139253.1.
DR AlphaFoldDB; Q8K5B3; -.
DR SMR; Q8K5B3; -.
DR STRING; 10116.ENSRNOP00000020328; -.
DR iPTMnet; Q8K5B3; -.
DR PhosphoSitePlus; Q8K5B3; -.
DR jPOST; Q8K5B3; -.
DR PaxDb; Q8K5B3; -.
DR GeneID; 246117; -.
DR KEGG; rno:246117; -.
DR UCSC; RGD:628690; rat.
DR CTD; 90411; -.
DR RGD; 628690; Mcfd2.
DR eggNOG; KOG4065; Eukaryota.
DR InParanoid; Q8K5B3; -.
DR OrthoDB; 1601131at2759; -.
DR PhylomeDB; Q8K5B3; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR PRO; PR:Q8K5B3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IDA:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..145
FT /note="Multiple coagulation factor deficiency protein 2
FT homolog"
FT /id="PRO_0000004161"
FT DOMAIN 67..102
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 115..145
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 145 AA; 16148 MW; 3B3670BB12C89AFF CRC64;
MASLQLLRGP FLCVLLWAFC VPGARAQEHG AGVHHGSVGL DKSTVHDQEH IMEHLEGVIN
QPEAEMSPQE LQLHYFKMHD YDGNSLLDGL ELSTAITHVH KEEGSEQVPP MSEDELISII
DGVLRDDDKN NDGYIDYAEF AKSLQ
